GenomeNet

Database: UniProt
Entry: A0A1S8TH62_9CLOT
LinkDB: A0A1S8TH62_9CLOT
Original site: A0A1S8TH62_9CLOT 
ID   A0A1S8TH62_9CLOT        Unreviewed;       441 AA.
AC   A0A1S8TH62;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Taurine--pyruvate aminotransferase {ECO:0000313|EMBL:OOM77140.1};
DE            EC=2.6.1.77 {ECO:0000313|EMBL:OOM77140.1};
GN   Name=tpa {ECO:0000313|EMBL:OOM77140.1};
GN   ORFNames=CLPUN_24550 {ECO:0000313|EMBL:OOM77140.1};
OS   Clostridium puniceum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM77140.1, ECO:0000313|Proteomes:UP000190890};
RN   [1] {ECO:0000313|EMBL:OOM77140.1, ECO:0000313|Proteomes:UP000190890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM77140.1,
RC   ECO:0000313|Proteomes:UP000190890};
RA   Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA   Daniel R.;
RT   "Microbial solvent formation.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOM77140.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LZZM01000154; OOM77140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8TH62; -.
DR   STRING; 29367.CLPUN_24550; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000190890; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OOM77140.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:OOM77140.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190890};
KW   Transferase {ECO:0000313|EMBL:OOM77140.1}.
SQ   SEQUENCE   441 AA;  49493 MW;  A7F7CA56D0045201 CRC64;
     MNGEEIKETL KKYNLQSWSK QRNINPIPVE KGEGIYFWDY EGNRYSDMSS QLVNMNLGFG
     NKEIADSIKG QVDKYCFVGP SYGAESRAKL AKKIIELMPD NMGKVFFTNA GAESNENAVK
     MARMFTGKTK VFSRYRSYHG SSFGAGNLTG EPRRYALEPG IPGFVKFFDP YIYREPIEFE
     SEEAATKYYL AKLREQIIYE GPDSIAAIVM ETITGSNGII IPPKGYLPGV RALCDEFKIL
     MICDEVMTGW GRTGKMFGFE NFGIKPDIVT FAKGVTCGYV QLGGAVVSKE IAEYFDDNLL
     SCGLTYSGHP LACAAGVACI NYYEKENILE NVNELGKVLG EKLEEMKDNH PCIGDVRYIG
     LFSAVELVKN KKTKEPLVPY GKDPEGIMVK IIGELKERRF MTYSHENMVL IAPPLIITKE
     QLEEELAKLD EVLEIVDKQF I
//
DBGET integrated database retrieval system